7n3j: Difference between revisions
New page: '''Unreleased structure''' The entry 7n3j is ON HOLD Authors: Description: Category: Unreleased Structures |
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==E. coli peptidyl-prolyl cis-trans isomerase, mutant Phe27CF3-Tyr/Phe98CF3-Tyr== | |||
<StructureSection load='7n3j' size='340' side='right'caption='[[7n3j]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7n3j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N3J FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=05O:(2S)-2-amino-3-[4-(trifluoromethoxy)phenyl]propanal'>05O</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n3j OCA], [https://pdbe.org/7n3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n3j RCSB], [https://www.ebi.ac.uk/pdbsum/7n3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n3j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PPIB_ECOLI PPIB_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fluorine atoms are known to display scalar (19)F-(19)F couplings in nuclear magnetic resonance (NMR) spectra when they are sufficiently close in space for nonbonding orbitals to overlap. We show that fluorinated noncanonical amino acids positioned in the hydrophobic core or on the surface of a protein can be linked by scalar through-space (19)F-(19)F ((TS)JFF) couplings even if the (19)F spins are in the time average separated by more than the van der Waals distance. Using two different aromatic amino acids featuring CF3 groups, O-trifluoromethyl-tyrosine and 4-trifluoromethyl-phenylalanine, we show that (19)F-(19)F TOCSY experiments are sufficiently sensitive to detect (TS)JFF couplings between 2.5 and 5 Hz in the 19 kDa protein PpiB measured on a two-channel 400 MHz NMR spectrometer with a regular room temperature probe. A quantitative J evolution experiment enables the measurement of (TS)JFF coupling constants that are up to five times smaller than the (19)F NMR line width. In addition, a new aminoacyl-tRNA synthetase was identified for genetic encoding of N(6)-(trifluoroacetyl)-l-lysine (TFA-Lys) and (19)F-(19)F TOCSY peaks were observed between two TFA-Lys residues incorporated into the proteins AncCDT-1 and mRFP despite high solvent exposure and flexibility of the TFA-Lys side chains. With the ready availability of systems for site-specific incorporation of fluorinated amino acids into proteins by genetic encoding, (19)F-(19)F interactions offer a straightforward way to probe the spatial proximity of selected sites without any assignments of (1)H NMR resonances. | |||
Through-Space Scalar (19)F-(19)F Couplings between Fluorinated Noncanonical Amino Acids for the Detection of Specific Contacts in Proteins.,Orton HW, Qianzhu H, Abdelkader EH, Habel EI, Tan YJ, Frkic RL, Jackson CJ, Huber T, Otting G J Am Chem Soc. 2021 Nov 24;143(46):19587-19598. doi: 10.1021/jacs.1c10104. Epub, 2021 Nov 15. PMID:34780162<ref>PMID:34780162</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7n3j" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Frkic RL]] | |||
[[Category: Jackson CJ]] | |||
[[Category: Otting G]] | |||
Latest revision as of 19:23, 18 October 2023
E. coli peptidyl-prolyl cis-trans isomerase, mutant Phe27CF3-Tyr/Phe98CF3-TyrE. coli peptidyl-prolyl cis-trans isomerase, mutant Phe27CF3-Tyr/Phe98CF3-Tyr
Structural highlights
FunctionPPIB_ECOLI PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Publication Abstract from PubMedFluorine atoms are known to display scalar (19)F-(19)F couplings in nuclear magnetic resonance (NMR) spectra when they are sufficiently close in space for nonbonding orbitals to overlap. We show that fluorinated noncanonical amino acids positioned in the hydrophobic core or on the surface of a protein can be linked by scalar through-space (19)F-(19)F ((TS)JFF) couplings even if the (19)F spins are in the time average separated by more than the van der Waals distance. Using two different aromatic amino acids featuring CF3 groups, O-trifluoromethyl-tyrosine and 4-trifluoromethyl-phenylalanine, we show that (19)F-(19)F TOCSY experiments are sufficiently sensitive to detect (TS)JFF couplings between 2.5 and 5 Hz in the 19 kDa protein PpiB measured on a two-channel 400 MHz NMR spectrometer with a regular room temperature probe. A quantitative J evolution experiment enables the measurement of (TS)JFF coupling constants that are up to five times smaller than the (19)F NMR line width. In addition, a new aminoacyl-tRNA synthetase was identified for genetic encoding of N(6)-(trifluoroacetyl)-l-lysine (TFA-Lys) and (19)F-(19)F TOCSY peaks were observed between two TFA-Lys residues incorporated into the proteins AncCDT-1 and mRFP despite high solvent exposure and flexibility of the TFA-Lys side chains. With the ready availability of systems for site-specific incorporation of fluorinated amino acids into proteins by genetic encoding, (19)F-(19)F interactions offer a straightforward way to probe the spatial proximity of selected sites without any assignments of (1)H NMR resonances. Through-Space Scalar (19)F-(19)F Couplings between Fluorinated Noncanonical Amino Acids for the Detection of Specific Contacts in Proteins.,Orton HW, Qianzhu H, Abdelkader EH, Habel EI, Tan YJ, Frkic RL, Jackson CJ, Huber T, Otting G J Am Chem Soc. 2021 Nov 24;143(46):19587-19598. doi: 10.1021/jacs.1c10104. Epub, 2021 Nov 15. PMID:34780162[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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